scholarly journals Identification and Characterization of a Major Zn(II) Resistance Determinant of Mycobacterium smegmatis

2006 ◽  
Vol 188 (19) ◽  
pp. 7026-7032 ◽  
Author(s):  
Amit Grover ◽  
Rakesh Sharma
Keyword(s):  
Mycobacterium Smegmatis ◽  
In Silico Analysis ◽  
Zinc Ion ◽  
Cation Diffusion ◽  
Cation Diffusion Facilitator ◽  
Transposon Insertion ◽  
Gene Coding ◽  
Family Protein ◽  
Opportunistic Pathogenic

ABSTRACT A zinc ion-sensitive mutant of Mycobacterium smegmatis was isolated. The transposon insertion was located in zitA (MSMEG0750), a gene coding for a cation diffusion facilitator family protein. Zinc ions specifically induced expression of zitA. In silico analysis revealed that environmental and opportunistic pathogenic species contain higher numbers of cation diffusion facilitator genes than do obligate pathogens.

scholarly journals The Cation Diffusion Facilitator Family Protein EmfA Confers Resistance to Manganese Toxicity in Brucella abortus 2308 and Is an Essential Virulence Determinant in Mice

2019 ◽  
Vol 202 (1) ◽  
Author(s):  
Matthew J. Johnsrude ◽  
Joshua E. Pitzer ◽  
Daniel W. Martin ◽  
R. Martin Roop
Keyword(s):  
Brucella Abortus ◽  
Manganese Toxicity ◽  
Cation Diffusion ◽  
Cation Diffusion Facilitator ◽  
Mn Toxicity ◽  
Virulence Determinant ◽  
Family Protein ◽  
Cellular Components ◽  
Cation Diffusion Facilitator Family

Mn nutrition is essential for the basic physiology and virulence of Brucella strains. The results of the study presented here demonstrate that the cation diffusion facilitator (CDF)-type metal exporter EmfA plays critical roles in maintaining Mn homeostasis and preventing Mn toxicity in Brucella and is an essential virulence determinant for these bacteria. EmfA and other cellular components involved in Mn homeostasis represent attractive targets for the development of improved vaccines and chemotherapeutic strategies for preventing and treating brucellosis in humans and animals.

Crystal structure of the cytosolic domain of the cation diffusion facilitator family protein

2009 ◽  
Vol 76 (3) ◽  
pp. 768-771 ◽  
Author(s):  
Takashi Higuchi ◽  
Motoyuki Hattori ◽  
Yoshiki Tanaka ◽  
Ryuichiro Ishitani ◽  
Osamu Nureki
Keyword(s):  
Crystal Structure ◽  
Cation Diffusion ◽  
Cation Diffusion Facilitator ◽  
Family Protein ◽  
Cytosolic Domain ◽  
Cation Diffusion Facilitator Family

ZnT-1 extrudes zinc from mammalian cells functioning as a Zn2+/H+exchanger

Metallomics ◽  
2014 ◽  
Vol 6 (9) ◽  
pp. 1656-1663 ◽  
Author(s):  
Eden Shusterman ◽  
Ofer Beharier ◽  
Levy Shiri ◽  
Raz Zarivach ◽  
Yoram Etzion ◽  
...  
Keyword(s):  
Phylogenetic Tree ◽  
Mammalian Cells ◽  
Cation Diffusion ◽  
Cation Diffusion Facilitator ◽  
Family Protein

ZnT-1 is a Cation Diffusion Facilitator (CDF) family protein, and is present throughout the phylogenetic tree from bacteria to humans.

Characterization of a Glomus intraradices gene encoding a putative Zn transporter of the cation diffusion facilitator family

2005 ◽  
Vol 42 (2) ◽  
pp. 130-140 ◽  
Author(s):  
Manuel González-Guerrero ◽  
Concepción Azcón-Aguilar ◽  
Michelle Mooney ◽  
Ascensión Valderas ◽  
Colin W. MacDiarmid ◽  
...  
Keyword(s):  
Glomus Intraradices ◽  
Cation Diffusion ◽  
Gene Encoding ◽  
Cation Diffusion Facilitator ◽  
Cation Diffusion Facilitator Family

scholarly journals In Silico Analysis of Coding/Noncoding SNPs of Human RETN Gene and Characterization of Their Impact on Resistin Stability and Structure

2019 ◽  
Vol 2019 ◽  
pp. 1-9 ◽  
Author(s):  
Lamiae Elkhattabi ◽  
Imane Morjane ◽  
Hicham Charoute ◽  
Soumaya Amghar ◽  
Hind Bouafi ◽  
...  
Keyword(s):  
3D Structure ◽  
In Silico Analysis ◽  
Metabolic Phenotype ◽  
Nucleotide Polymorphisms ◽  
Coding Region ◽  
Single Nucleotide ◽  
Functional Studies ◽  
Gene Coding ◽  
Human Resistin

Resistin (RETN) is a gene coding for proinflammatory adipokine called resistin secreted by macrophages in humans. Single nucleotide polymorphisms (SNPs) in RETN are linked to obesity and insulin resistance in various populations. Using dbSNP, 78 nonsynonymous SNPs (nsSNPs) were retrieved and tested on a PredictSNP 1.0 megaserver. Among these, 15 nsSNPs were predicted as highly deleterious and thus subjected to further analyses, such as conservation, posttranscriptional modifications, and stability. The 3D structure of human resistin was generated by homology modeling using Swiss model. Root-mean-square deviation (RMSD), hydrogen bonds (h-bonds), and interactions were estimated. Furthermore, UTRscan served to identify UTR functional SNPs. Among the 15 most deleterious nsSNPs, 13 were predicted to be highly conserved including variants in posttranslational modification sites. Stability analysis predicted 9 nsSNPs (I32S, C51Y, G58E, G58R, C78S, G79C, W98C, C103G, and C104Y) which can decrease protein stability with at least three out of the four algorithms used in this study. These nsSNPs were chosen for structural analysis. Both variants C51Y and C104Y showed the highest RMS deviations (1.137 Å and 1.308 Å, respectively) which were confirmed by the important decrease in total h-bonds. The analysis of hydrophobic and hydrophilic interactions showed important differences between the native protein and the 9 mutants, particularly I32S, G79C, and C104Y. Six SNPs in the 3′UTR (rs920569876, rs74176247, rs1447199134, rs943234785, rs76346269, and rs78048640) were predicted to be implicated in polyadenylation signal. This study revealed 9 highly deleterious SNPs located in the human RETN gene coding region and 6 SNPs within the 3′UTR that may alter the protein structure. Interestingly, these SNPs are worth to be analyzed in functional studies to further elucidate their effect on metabolic phenotype occurrence.

scholarly journals Glycopeptidolipid Acetylation Affects Sliding Motility and Biofilm Formation in Mycobacterium smegmatis

2001 ◽  
Vol 183 (19) ◽  
pp. 5718-5724 ◽  
Author(s):  
Judith Recht ◽  
Roberto Kolter
Keyword(s):  
Polyvinyl Chloride ◽  
Mycobacterium Smegmatis ◽  
Biofilm Formation ◽  
Physical Characterization ◽  
Colony Morphology ◽  
Partial Inhibition ◽  
Transposon Insertion ◽  
Biosynthesis Gene ◽  
Sliding Motility

ABSTRACT The absence of glycopeptidolipids (GPLs) abolishes the ability of mycobacteria both to slide over the surface of motility plates and to form biofilms on polyvinyl chloride. In a screen for biofilm-defective mutants of Mycobacterium smegmatis mc2155, a new mutant was obtained that resulted in partial inhibition of both processes and also showed an intermediate rough colony morphology. Themariner transposon insertion mapped to a GPL biosynthesis gene (atf1) which encodes a putative acetyltranferase involved in the transfer of acetyl groups to the glycopeptide core. Physical characterization of the GPLs from the atf1 mutant demonstrated that they were not acetylated.

scholarly journals Roles of Lsr2 in Colony Morphology and Biofilm Formation of Mycobacterium smegmatis

2006 ◽  
Vol 188 (2) ◽  
pp. 633-641 ◽  
Author(s):  
Jeffrey M. Chen ◽  
Greg J. German ◽  
David C. Alexander ◽  
Huiping Ren ◽  
Tracy Tan ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mycobacterium Smegmatis ◽  
Biofilm Formation ◽  
Mycolic Acid ◽  
Colony Morphology ◽  
Insertion Mutant ◽  
Transposon Insertion ◽  
Layer Chromatography ◽  
Wall Components

ABSTRACT The lipid-rich cell wall is a defining feature of Mycobacterium species. Individual cell wall components affect diverse mycobacterial phenotypes including colony morphology, biofilm formation, antibiotic resistance, and virulence. In this study, we describe a transposon insertion mutant of Mycobacterium smegmatis mc2155 that exhibits altered colony morphology and defects in biofilm formation. The mutation was localized to the lsr2 gene. First identified as an immunodominant T-cell antigen of Mycobacterium leprae, lsr2 orthologs have been identified in all sequenced mycobacterial genomes, and homologs are found in many actinomycetes. Although its precise function remains unknown, localization experiments indicate that Lsr2 is a cytosolic protein, and cross-linking experiments demonstrate that it exists as a dimer. Characterization of cell wall lipid components reveals that the M. smegmatis lsr2 mutant lacks two previously unidentified apolar lipids. Characterization by mass spectrometry and thin-layer chromatography indicate that these two apolar lipids are novel mycolate-containing compounds, called mycolyl-diacylglycerols (MDAGs), in which a mycolic acid (α- or α′-mycolate) molecule is esterified to a glycerol. Upon complementation with an intact lsr2 gene, the mutant reverts to the parental phenotypes and MDAG production is restored. This study demonstrates that due to its impact on the biosynthesis of the hydrophobic MDAGs, Lsr2 plays an important role in the colony morphology and biofilm formation of M. smegmatis.

scholarly journals Attenuated Signature-Tagged Mutagenesis Mutants ofBrucella melitensis Identified during the Acute Phase ofInfection inMice

2003 ◽  
Vol 71 (12) ◽  
pp. 7053-7060 ◽  
Author(s):  
P. Lestrate ◽  
A. Dricot ◽  
R.-M. Delrue ◽  
C. Lambert ◽  
V. Martinelli ◽  
...  
Keyword(s):  
Mouse Model ◽  
Molecular Mechanisms ◽  
Brucella Melitensis ◽  
Functional Protein ◽  
Transposon Insertion ◽  
Gene Coding ◽  
Insertion Sites ◽  
Mouse Model Of Infection

ABSTRACT For this study, we screened 1,152 signature-tagged mutagenesis mutants of Brucella melitensis 16M in a mouse model of infection and found 36 of them to be attenuated in vivo. Molecular characterization of transposon insertion sites showed that for four mutants, the affected genes were only present in Rhizobiaceae. Another mutant contained a disruption in a gene homologous to mosA, which is involved in rhizopine biosynthesis in some strains of Rhizobium, suggesting that this sugar may be involved in Brucella pathogenicity. A mutant was disrupted in a gene homologous to fliF, a gene potentially coding for the MS ring, a basal component of the flagellar system. Surprisingly, a mutant was affected in the rpoA gene, coding for the essentialα -subunit of the RNA polymerase. This disruption leaves a partially functional protein, impaired for the activation of virB transcription, as demonstrated by the absence of induction of the virB promoter in the Tn5::rpoA background. The results presented here highlight the fact that the ability of Brucella to induce pathogenesis shares similarities with the molecular mechanisms used by both Rhizobium and Agrobacterium to colonize their hosts.

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